MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold protein TANC1

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• 作者：Hideo Nonaka ; Kimiko Takei ; Masato Umikawa ; Minoru Oshiro ; Kouichi Kuninaka ; Maitsetseg Bayarjargal ; Tsuyoshi Asato ; Yoshito Yamashiro ; Yukiko Uechi ; Shogo Endo ; Tatsuo Suzuki ; Ken-ichi Kariya
• 关键词：Rap2 ; Rap1 ; Ras ; Small G protein ; MINK ; TNIK ; Mitogen-activated protein kinase kinase kinase kinase ; TANC1 ; Postsynaptic scaffold protein
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2008
• 出版时间：12 December 2008
• 年：2008
• 卷：377
• 期：2
• 页码：573-578
• 全文大小：510 K

文摘

Rap1 and Rap2 are similar Ras-like G proteins but perform distinct functions. By the affinity chromatography/mass-spectrometry approach and the yeast two-hybrid screening, we identified Misshapen/NIKs-related kinase (MINK) as a novel Rap2-interacting protein that does not interact with Rap1 or Ras. MINK is a member of the STE20 group of mitogen-activated protein kinase kinase kinase kinases. The interaction between MINK and Rap2 was GTP-dependent and required Phe39 within the effector region of Rap2; the corresponding residue in Rap1 and Ras is Ser. MINK was enriched in the brain, and both MINK and its close relative, Traf2- and Nck-interacting kinase (TNIK), interacted with a postsynaptic scaffold protein containing tetratricopeptide repeats, ankyrin repeats and a coiled-coil region (TANC1) and induced its phosphorylation, under control of Rap2 in cultured cells. These are novel actions of MINK and TNIK, and consistent with a role of MINK as a Rap2 effector in the brain.